InterPro domain: IPR013209

This domain is found in lipins and lipin homologues from Saccharomyces cerevisiae (Smp2) and from Schizosaccharomyces pombe (Ned1) [ 1 ]. Smp2 (also known as PAH1) is involved in plasmid maintenance and respiration [ 2 ] and has been identified as a Mg2+-dependent phosphatidate phosphatase ( 3.1.3.4 ) that contains a haloacid dehalogenase (HAD)-like domain [ 2 ]. Lipin proteins are phosphatidate phosphatases which catalyse the dephosphorylation of phosphatidic acid to diacylglycerol, the penultimate step in triacylglycerol synthesis [ 3 ]. They are involved in adipose tissue development and insulin resistance [ 4 ].

1. An evolutionarily conserved fission yeast protein, Ned1, implicated in normal nuclear morphology and chromosome stability, interacts with Dis3, Pim1/RCC1 and an essential nucleoporin. J. Cell. Sci. 115, 4375-85
2. The Saccharomyces cerevisiae Lipin homolog is a Mg2+-dependent phosphatidate phosphatase enzyme. J. Biol. Chem. 281, 9210-8
3. Lipins, lipinopathies, and the modulation of cellular lipid storage and signaling. Prog. Lipid Res. 52, 305-16
4. Insulin-stimulated phosphorylation of lipin mediated by the mammalian target of rapamycin. Proc. Natl. Acad. Sci. U.S.A. 99, 1047-52